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Titolo:
Halenaquinol, a natural cardioactive pentacyclic hydroquinone, interacts with sulfhydryls on rat brain Na+,K+-ATPase
Autore:
Gorshkova, IA; Gorshkov, BA; Fedoreev, SA; Stonik, VA;
Indirizzi:
Russian Acad Sci, Pacific Inst Bioorgan Chem, Far E Branch, Vladivostok 690022, Russia Russian Acad Sci Vladivostok Russia 690022 h, Vladivostok 690022, Russia
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY
fascicolo: 4, volume: 128, anno: 2001,
pagine: 531 - 540
SICI:
1532-0456(200104)128:4<531:HANCPH>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
MARINE SPONGE; OUABAIN BINDING; ATPASE; INHIBITION; (NA,K)-ATPASE; SULFATE; SITE; IDENTIFICATION; XESTOQUINONE; NA,K-PUMP;
Keywords:
halenaquinol; inhibition; marine natural products; Na +, K+-ATPase; rat brain; sponge; sulfhydryls; Petrosia seriata;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Gorshkova, IA Russian Acad Sci, Pacific Inst Bioorgan Chem, Far E Branch, Vladivostok 690022, Russia Russian Acad Sci Vladivostok Russia 690022 690022, Russia
Citazione:
I.A. Gorshkova et al., "Halenaquinol, a natural cardioactive pentacyclic hydroquinone, interacts with sulfhydryls on rat brain Na+,K+-ATPase", COMP BIOC C, 128(4), 2001, pp. 531-540

Abstract

Halenaquinol inhibited the partial reactions of ATP hydrolysis by rat brain cortex Na+,K+-ATPase, such as [H-3]ATP binding to the enzyme. Na+-dependent front-door phosphorylation from [gamma-P-33]ATP, and also Na+- and K+-dependent E-1 <----> E-2 conformational transitions of the enzyme. Halenaquinol abolished the positive cooperativity between the Na+- and K+-binding sites on the enzyme. ATP and sulfhydryl-containing reagents (cysteine and dithiothreitol) protected the Na+,K+-ATPase against inhibition, Halenaquinol can react with additional vital groups in the enzyme after blockage of certain sulfhydryl groups with 5,5'-dithio-bis-nitrobenzoic acid. Halenaquinol inhibited [H-3]ouabain binding to Na+,K+-ATPase under phosphorylating and non-phosphorylating conditions. Binding of fluorescein 5'-isothiocyanate to Na,K+-ATPase and intensity of fluorescence of enzyme tryptophanyl residues were decreased by halenaquinol. We suggest that interaction of halenaquinol with the essential sulfhydryls in/or near the ATP-binding site of Na+,K+-ATPase resulted in a change of protein conformation and subsequent alterationof overall and partial enzymatic reactions, (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 10:22:49